. "R\u00E1zga, Filip" . . "Adenine Press" . "Ko\u010Da, Jaroslav" . . "\u0160poner, Ji\u0159\u00ED" . "RIV/00216224:14310/05:00013831!RIV06-MSM-14310___" . "Elbow-like motions in Ribosomal Kink-turns: The role of the second A-minor motif and Nominally unpaired bases"@en . . "[B29AC9864289]" . . "14310" . "800-801" . . "Journal Of Biomolecular Structure and Dynamics" . "Kink-turn (K-turn) motifs are asymmetric internal loops found at conserved positions in diverse RNAs, with sharp bends in phosphodiester backbones producing %22V%22-shaped structures. Explicit-solvent Molecular Dynamics (MD) simulations were carried out for selected K-turns from 23S rRNA (Kt-38, Kt-42, Kt-58) and for K-turn of human U4 snRNA (Kt-U4). The MD simulations reveal hinge-like K-turn motions on the nanosecond time-scale and thus indicate that K-turns are dynamically flexible, and capable of regulating significant inter-segmental motions. The first conserved A-minor interaction between the K-turn stems is entirely stable in all simulations. The angle between the helical arms of Kt-38 and Kt-42 is regulated by local variations of the second A-minor (type I) interaction between the stems. Its variability ranges from closed geometries to open ones stabilized by insertion of long-residency waters between adenine and cytosine. Kt-58 and Kt-U4 exhibit similar elbow-like motions caused by conformationa" . . "Klbove pohyby Ribosomalnych Kink turnov: Uloha druhej A-minor interakcie a nesparenych nukleotidov"@cs . "Elbow-like motions in Ribosomal Kink-turns: The role of the second A-minor motif and Nominally unpaired bases" . "3"^^ . "2005-01-01+01:00"^^ . . . "2"^^ . "Leontis, Neocles B." . "4"^^ . . . . "Elbow-like motions in Ribosomal Kink-turns: The role of the second A-minor motif and Nominally unpaired bases" . . "Kink-turn; RNA flexibility; A-minor; Ribosome dynamics"@en . "New York, USA" . "1533-0346" . "Kink-turn (K-turn) motifs are asymmetric internal loops found at conserved positions in diverse RNAs, with sharp bends in phosphodiester backbones producing %22V%22-shaped structures. Explicit-solvent Molecular Dynamics (MD) simulations were carried out for selected K-turns from 23S rRNA (Kt-38, Kt-42, Kt-58) and for K-turn of human U4 snRNA (Kt-U4). The MD simulations reveal hinge-like K-turn motions on the nanosecond time-scale and thus indicate that K-turns are dynamically flexible, and capable of regulating significant inter-segmental motions. The first conserved A-minor interaction between the K-turn stems is entirely stable in all simulations. The angle between the helical arms of Kt-38 and Kt-42 is regulated by local variations of the second A-minor (type I) interaction between the stems. Its variability ranges from closed geometries to open ones stabilized by insertion of long-residency waters between adenine and cytosine. Kt-58 and Kt-U4 exhibit similar elbow-like motions caused by conformationa"@cs . . "Klbove pohyby Ribosomalnych Kink turnov: Uloha druhej A-minor interakcie a nesparenych nukleotidov"@cs . "RIV/00216224:14310/05:00013831" . "Elbow-like motions in Ribosomal Kink-turns: The role of the second A-minor motif and Nominally unpaired bases"@en . "Albany, NY, USA" . . . "Kink-turn (K-turn) motifs are asymmetric internal loops found at conserved positions in diverse RNAs, with sharp bends in phosphodiester backbones producing %22V%22-shaped structures. Explicit-solvent Molecular Dynamics (MD) simulations were carried out for selected K-turns from 23S rRNA (Kt-38, Kt-42, Kt-58) and for K-turn of human U4 snRNA (Kt-U4). The MD simulations reveal hinge-like K-turn motions on the nanosecond time-scale and thus indicate that K-turns are dynamically flexible, and capable of regulating significant inter-segmental motions. The first conserved A-minor interaction between the K-turn stems is entirely stable in all simulations. The angle between the helical arms of Kt-38 and Kt-42 is regulated by local variations of the second A-minor (type I) interaction between the stems. Its variability ranges from closed geometries to open ones stabilized by insertion of long-residency waters between adenine and cytosine. Kt-58 and Kt-U4 exhibit similar elbow-like motions caused by conformationa"@en . "P(LN00A016)" . . . . "519858" .